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Conserved domains on  [gi|119672920|ref|NP_659162|]
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7SK snRNA methylphosphate capping enzyme isoform 1 [Mus musculus]

Protein Classification

methylphosphate capping enzyme( domain architecture ID 10118155)

methylphosphate capping enzyme similar to Mus musculus 7SK snRNA methylphosphate capping enzyme which acts as a S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA (7SK RNA), leading to stabilize it

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
552-660 3.08e-65

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


:

Pssm-ID: 462022  Cd Length: 109  Bit Score: 210.09  E-value: 3.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  552 YDVVLCFSLTKWVHLNWGDEGLKRMFRRIYRHLRPGGILVLEPQPWSSYCKRKSLTETIYKNYFRIQLKPEQFSSYLTSp 631
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLS- 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 119672920  632 EVGFSSYELVA-TPNNTSRGFQRPVYLFHK 660
Cdd:pfam06859  80 EVGFESVEELGsTPEGKSKGFDRPIYLFRK 109
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
423-593 7.48e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


:

Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 59.37  E-value: 7.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 423 DVLDLGCNVGHLTLSIAcKWGPARMVGLDIDPRLIHSARQNIRHYLseelrlqaqtsegdpgtegeegtitvrkrscfpa 502
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALL---------------------------------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 503 sltasrgpiaapqvpldgadtsvfPNNVVFVTGNYvldrDELVDAQRPEYDVVLCFSLTKWVHLNWgdeglKRMFRRIYR 582
Cdd:cd02440   46 ------------------------ADNVEVLKGDA----EELPPEADESFDVIISDPPLHHLVEDL-----ARFLEEARR 92
                        170
                 ....*....|.
gi 119672920 583 HLRPGGILVLE 593
Cdd:cd02440   93 LLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
552-660 3.08e-65

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


Pssm-ID: 462022  Cd Length: 109  Bit Score: 210.09  E-value: 3.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  552 YDVVLCFSLTKWVHLNWGDEGLKRMFRRIYRHLRPGGILVLEPQPWSSYCKRKSLTETIYKNYFRIQLKPEQFSSYLTSp 631
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLS- 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 119672920  632 EVGFSSYELVA-TPNNTSRGFQRPVYLFHK 660
Cdd:pfam06859  80 EVGFESVEELGsTPEGKSKGFDRPIYLFRK 109
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
423-593 7.48e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 59.37  E-value: 7.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 423 DVLDLGCNVGHLTLSIAcKWGPARMVGLDIDPRLIHSARQNIRHYLseelrlqaqtsegdpgtegeegtitvrkrscfpa 502
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALL---------------------------------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 503 sltasrgpiaapqvpldgadtsvfPNNVVFVTGNYvldrDELVDAQRPEYDVVLCFSLTKWVHLNWgdeglKRMFRRIYR 582
Cdd:cd02440   46 ------------------------ADNVEVLKGDA----EELPPEADESFDVIISDPPLHHLVEDL-----ARFLEEARR 92
                        170
                 ....*....|.
gi 119672920 583 HLRPGGILVLE 593
Cdd:cd02440   93 LLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
420-593 1.90e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 57.91  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 420 QGRDVLDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSARQNIrhylseelrlqaqtsegdPGTEGEEGTITvrkrsc 499
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL------------------PNVRFVVADLR------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 500 fpasltasrgpiaapQVPLDGadtsvfpnnvvfvtgnyvldrdelvdaqrpEYDVVLCFSLTKWVhlnwgdEGLKRMFRR 579
Cdd:COG4106   57 ---------------DLDPPE------------------------------PFDLVVSNAALHWL------PDHAALLAR 85
                        170
                 ....*....|....
gi 119672920 580 IYRHLRPGGILVLE 593
Cdd:COG4106   86 LAAALAPGGVLAVQ 99
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
424-588 7.50e-10

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 7.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  424 VLDLGCNVGHLTLSIAcKWGPARMVGLDIDPRLIHSARQNIRhylseELRLQAQTSEGDpgtegeegtitvrkrscfpas 503
Cdd:pfam13649   1 VLDLGCGTGRLTLALA-RRGGARVTGVDLSPEMLERARERAA-----EAGLNVEFVQGD--------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  504 ltasrgpiaAPQVPldgadtsvFPNNvvfvtgnyvldrdelvdaqrpEYDVVLCFSLtkWVHLNWGDegLKRMFRRIYRH 583
Cdd:pfam13649  54 ---------AEDLP--------FPDG---------------------SFDLVVSSGV--LHHLPDPD--LEAALREIARV 91

                  ....*
gi 119672920  584 LRPGG 588
Cdd:pfam13649  92 LKPGG 96
PLN02672 PLN02672
methionine S-methyltransferase
419-495 2.03e-06

methionine S-methyltransferase


Pssm-ID: 215360 [Multi-domain]  Cd Length: 1082  Bit Score: 51.31  E-value: 2.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119672920  419 FQGRDVLDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSARQNirhylseeLRLQAQTSEGDPGTEGEEGTITVR 495
Cdd:PLN02672  117 FRDKTVAELGCGNGWISIAIAEKWLPSKVYGLDINPRAVKVAWIN--------LYLNALDDDGLPVYDGEGKTLLDR 185
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
552-660 3.08e-65

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


Pssm-ID: 462022  Cd Length: 109  Bit Score: 210.09  E-value: 3.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  552 YDVVLCFSLTKWVHLNWGDEGLKRMFRRIYRHLRPGGILVLEPQPWSSYCKRKSLTETIYKNYFRIQLKPEQFSSYLTSp 631
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLS- 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 119672920  632 EVGFSSYELVA-TPNNTSRGFQRPVYLFHK 660
Cdd:pfam06859  80 EVGFESVEELGsTPEGKSKGFDRPIYLFRK 109
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
423-593 7.48e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 59.37  E-value: 7.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 423 DVLDLGCNVGHLTLSIAcKWGPARMVGLDIDPRLIHSARQNIRHYLseelrlqaqtsegdpgtegeegtitvrkrscfpa 502
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALL---------------------------------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 503 sltasrgpiaapqvpldgadtsvfPNNVVFVTGNYvldrDELVDAQRPEYDVVLCFSLTKWVHLNWgdeglKRMFRRIYR 582
Cdd:cd02440   46 ------------------------ADNVEVLKGDA----EELPPEADESFDVIISDPPLHHLVEDL-----ARFLEEARR 92
                        170
                 ....*....|.
gi 119672920 583 HLRPGGILVLE 593
Cdd:cd02440   93 LLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
420-593 1.90e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 57.91  E-value: 1.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 420 QGRDVLDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSARQNIrhylseelrlqaqtsegdPGTEGEEGTITvrkrsc 499
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL------------------PNVRFVVADLR------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 500 fpasltasrgpiaapQVPLDGadtsvfpnnvvfvtgnyvldrdelvdaqrpEYDVVLCFSLTKWVhlnwgdEGLKRMFRR 579
Cdd:COG4106   57 ---------------DLDPPE------------------------------PFDLVVSNAALHWL------PDHAALLAR 85
                        170
                 ....*....|....
gi 119672920 580 IYRHLRPGGILVLE 593
Cdd:COG4106   86 LAAALAPGGVLAVQ 99
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
424-588 7.50e-10

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.03  E-value: 7.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  424 VLDLGCNVGHLTLSIAcKWGPARMVGLDIDPRLIHSARQNIRhylseELRLQAQTSEGDpgtegeegtitvrkrscfpas 503
Cdd:pfam13649   1 VLDLGCGTGRLTLALA-RRGGARVTGVDLSPEMLERARERAA-----EAGLNVEFVQGD--------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  504 ltasrgpiaAPQVPldgadtsvFPNNvvfvtgnyvldrdelvdaqrpEYDVVLCFSLtkWVHLNWGDegLKRMFRRIYRH 583
Cdd:pfam13649  54 ---------AEDLP--------FPDG---------------------SFDLVVSSGV--LHHLPDPD--LEAALREIARV 91

                  ....*
gi 119672920  584 LRPGG 588
Cdd:pfam13649  92 LKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
408-593 5.98e-08

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 51.56  E-value: 5.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 408 DVRL-RVLKPEWFQGRDVLDLGCNVGHLTLSIAcKWGpARMVGLDIDPRLIHSARQNIRHYlseelrlqaqtsegdpgte 486
Cdd:COG2227   11 DRRLaALLARLLPAGGRVLDVGCGTGRLALALA-RRG-ADVTGVDISPEALEIARERAAEL------------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 487 geegtitvrkrscfpasltasrgpiaapqvpldgadtsvfpnNVVFVTGNYvldrdELVDAQRPEYDVVLCFSltkwV-- 564
Cdd:COG2227   70 ------------------------------------------NVDFVQGDL-----EDLPLEDGSFDLVICSE----Vle 98
                        170       180
                 ....*....|....*....|....*....
gi 119672920 565 HLnwgdEGLKRMFRRIYRHLRPGGILVLE 593
Cdd:COG2227   99 HL----PDPAALLRELARLLKPGGLLLLS 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
398-594 7.44e-08

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 53.00  E-value: 7.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 398 YYGYRNPSCEDVRLRVLKPEwfQGRDVLDLGCNVGHLTLSIACKWGpARMVGLDIDPRLIHSARQNIRHYlseelrlqaq 477
Cdd:COG0500    6 YSDELLPGLAALLALLERLP--KGGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARARAAKA---------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 478 tsegdpgtegeegtitvrkrscfpasltasrgpiaapqvpldgadtsvFPNNVVFVTGNYvldrDELVDAQRPEYDVVLC 557
Cdd:COG0500   73 ------------------------------------------------GLGNVEFLVADL----AELDPLPAESFDLVVA 100
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 119672920 558 FSLtkWVHLNwgDEGLKRMFRRIYRHLRPGGILVLEP 594
Cdd:COG0500  101 FGV--LHHLP--PEEREALLRELARALKPGGVLLLSA 133
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
421-592 9.96e-07

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 48.45  E-value: 9.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 421 GRDVLDLGCNVGHLTLSIAcKWGpARMVGLDIDPRLIHSARQNIRhylseELRLQAQTSEGDpgtegeegtitvrkrscf 500
Cdd:COG2226   23 GARVLDLGCGTGRLALALA-ERG-ARVTGVDISPEMLELARERAA-----EAGLNVEFVVGD------------------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 501 pasltasrgpiaAPQVPldgadtsvFPNNvvfvtgnyvldrdelvdaqrpEYDVVLCFsltkWVHLNWGDegLKRMFRRI 580
Cdd:COG2226   78 ------------AEDLP--------FPDG---------------------SFDLVISS----FVLHHLPD--PERALAEI 110
                        170
                 ....*....|..
gi 119672920 581 YRHLRPGGILVL 592
Cdd:COG2226  111 ARVLKPGGRLVV 122
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
425-590 1.20e-06

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 47.36  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  425 LDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSARQNIRHYLseelrlqaqtsegdpgtegeegtitvrkrscfpasl 504
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALG------------------------------------ 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  505 tasrgpiaapqvpldgadtsvfPNNVVFVTGNyVLDRDELVDAQrpeYDVVLCFSltkwVHLNWGDegLKRMFRRIYRHL 584
Cdd:pfam08242  45 ----------------------LLNAVRVELF-QLDLGELDPGS---FDVVVASN----VLHHLAD--PRAVLRNIRRLL 92

                  ....*.
gi 119672920  585 RPGGIL 590
Cdd:pfam08242  93 KPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
424-477 1.99e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 47.80  E-value: 1.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 119672920  424 VLDLGCNVGHLTLSIACKWGP-ARMVGLDIDPRLIHSARQNIRHYLSEELRLQAQ 477
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELGPnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQG 61
PLN02672 PLN02672
methionine S-methyltransferase
419-495 2.03e-06

methionine S-methyltransferase


Pssm-ID: 215360 [Multi-domain]  Cd Length: 1082  Bit Score: 51.31  E-value: 2.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119672920  419 FQGRDVLDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSARQNirhylseeLRLQAQTSEGDPGTEGEEGTITVR 495
Cdd:PLN02672  117 FRDKTVAELGCGNGWISIAIAEKWLPSKVYGLDINPRAVKVAWIN--------LYLNALDDDGLPVYDGEGKTLLDR 185
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
414-592 2.16e-06

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.00  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 414 LKPewfqGRDVLDLGCNVGHLTLSIACKWGpARMVGLDIDPRLIHSARQNIRhylseelrlqaqtsegdpgtegEEGtit 493
Cdd:COG2230   49 LKP----GMRVLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAA----------------------EAG--- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 494 vrkrscfpasltasrgpiaapqvpldgadtsvFPNNVVFVTGNYvldRDELVDAQrpeYDVVLCFSLTKWVhlnwGDEGL 573
Cdd:COG2230   99 --------------------------------LADRVEVRLADY---RDLPADGQ---FDAIVSIGMFEHV----GPENY 136
                        170
                 ....*....|....*....
gi 119672920 574 KRMFRRIYRHLRPGGILVL 592
Cdd:COG2230  137 PAYFAKVARLLKPGGRLLL 155
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
421-592 1.19e-05

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 46.34  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 421 GRDVLDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSARQNirhylseelrlqaqtsegdpgtegeegtitvrkrscf 500
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARAN------------------------------------- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 501 pasltasrgpIAAPQVPldgadtsvfpnNVVFVTGNyVLDRdelVDAQRpeYDVVLC---FSltkwVHLNWGDEGLKRMF 577
Cdd:COG2813   93 ----------AAANGLE-----------NVEVLWSD-GLSG---VPDGS--FDLILSnppFH----AGRAVDKEVAHALI 141
                        170
                 ....*....|....*
gi 119672920 578 RRIYRHLRPGGILVL 592
Cdd:COG2813  142 ADAARHLRPGGELWL 156
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
419-465 1.68e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 46.05  E-value: 1.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119672920 419 FQGRDVLDLGCNVGhlTLSIACKW-GPARMVGLDIDPRLIHSARQNIR 465
Cdd:COG2263   44 IEGKTVLDLGCGTG--MLAIGAALlGAKKVVGVDIDPEALEIARENAE 89
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
420-466 4.90e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 45.14  E-value: 4.90e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 119672920 420 QGRDVLDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSARQNIRH 466
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVAL 83
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
419-465 8.82e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 44.78  E-value: 8.82e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119672920 419 FQGRDVLDLGCnvGhlT--LSIAC-KWGPARMVGLDIDPRLIHSARQNIR 465
Cdd:COG2264  147 KPGKTVLDVGC--G--SgiLAIAAaKLGAKRVLAVDIDPVAVEAARENAE 192
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
421-471 1.92e-04

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 42.63  E-value: 1.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119672920 421 GRDVLDLGCNVGhlTLSIACKWGPARMVGLDIDPRLIHSARQNIRHYLSEE 471
Cdd:COG1041   27 GDTVLDPFCGTG--TILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED 75
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
412-464 3.59e-04

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 43.02  E-value: 3.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119672920  412 RVLKPewfqGRDVLDLGCNVGhlTLSIAC-KWGPARMVGLDIDPRLIHSARQNI 464
Cdd:pfam06325 157 RLVKP----GESVLDVGCGSG--ILAIAAlKLGAKKVVGVDIDPVAVRAAKENA 204
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
421-465 6.02e-04

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 41.04  E-value: 6.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 119672920  421 GRDVLDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSARQNIR 465
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLA 76
PRK08317 PRK08317
hypothetical protein; Provisional
424-482 6.05e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 41.85  E-value: 6.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 424 VLDLGCNVGHLTLSIACKWGPA-RMVGLDIDPRLIHSARQNIrhylsEELRLQAQTSEGD 482
Cdd:PRK08317  23 VLDVGCGPGNDARELARRVGPEgRVVGIDRSEAMLALAKERA-----AGLGPNVEFVRGD 77
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
400-592 1.08e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 40.37  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 400 GYRNPscEDVRLRVLKP-EWFQGRDVLDLGCNVGHLTLSIAcKWGpARMVGLDIDPRLIHSARQNirhylseelrlqaqt 478
Cdd:COG4976   27 GYEAP--ALLAEELLARlPPGPFGRVLDLGCGTGLLGEALR-PRG-YRLTGVDLSEEMLAKAREK--------------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920 479 segdpgtegeegtitvrkrscfpasltasrgpiaapqvpldgadtsvfpnnvvfvtGNYV-LDRDELVDAQRPE--YDVV 555
Cdd:COG4976   88 --------------------------------------------------------GVYDrLLVADLADLAEPDgrFDLI 111
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 119672920 556 LCF-SLTkwvhlNWGDegLKRMFRRIYRHLRPGGILVL 592
Cdd:COG4976  112 VAAdVLT-----YLGD--LAAVFAGVARALKPGGLFIF 142
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
425-592 1.39e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 38.41  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  425 LDLGCNVGHLTLSIAcKWGPaRMVGLDIDPRLIHSARQNIRhylseelrlqaqtsegDPGTEGEEGTITvrkrscfpasl 504
Cdd:pfam08241   1 LDVGCGTGLLTELLA-RLGA-RVTGVDISPEMLELAREKAP----------------REGLTFVVGDAE----------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119672920  505 tasrgpiaapQVPLdgADTSVfpnnvvfvtgnyvldrdelvdaqrpeyDVVLCFSLTKWVHLnwgdegLKRMFRRIYRHL 584
Cdd:pfam08241  52 ----------DLPF--PDNSF---------------------------DLVLSSEVLHHVED------PERALREIARVL 86

                  ....*...
gi 119672920  585 RPGGILVL 592
Cdd:pfam08241  87 KPGGILII 94
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
419-465 1.72e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 40.52  E-value: 1.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119672920 419 FQGRDVLDLGCNVGhlTLSIAC-KWGPARMVGLDIDPRLIHSARQNIR 465
Cdd:PRK00517 118 LPGKTVLDVGCGSG--ILAIAAaKLGAKKVLAVDIDPQAVEAARENAE 163
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
398-466 2.15e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 39.33  E-value: 2.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119672920  398 YYGYRNPSCEDVRLRVLKPEWfQGRDVLDLGCNVGHLTLSIAcKWGPaRMVGLDIDPRLIHSARQNIRH 466
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLP-SPGRVLDFGCGTGIFLRLLR-AQGF-SVTGVDPSPIAIERALLNVRF 66
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
421-461 2.22e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 40.44  E-value: 2.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 119672920 421 GRDVLDLGCNVGHLTLSIACKWGPARMVGLDIDPRLIHSAR 461
Cdd:PRK14103  30 ARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAAR 70
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
418-466 3.61e-03

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 39.48  E-value: 3.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119672920 418 WFQGRDVLDLGCNVGhLTlSIAC-KWGPARMVGLDIDPRLIHSARQNIRH 466
Cdd:COG3897   68 EVAGKRVLELGCGLG-LV-GIAAaKAGAADVTATDYDPEALAALRLNAAL 115
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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